FLNA_HUMAN
ID FLNA_HUMAN Reviewed; 2647 AA.
AC P21333; E9KL45; Q5HY53; Q5HY55; Q8NF52;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 261.
DE RecName: Full=Filamin-A;
DE Short=FLN-A;
DE AltName: Full=Actin-binding protein 280;
DE Short=ABP-280;
DE AltName: Full=Alpha-filamin;
DE AltName: Full=Endothelial actin-binding protein;
DE AltName: Full=Filamin-1;
DE AltName: Full=Non-muscle filamin;
GN Name=FLNA; Synonyms=FLN, FLN1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2391361; DOI=10.1083/jcb.111.3.1089;
RA Gorlin J.B., Yamin R., Egan S., Stewart M., Stossel T.P., Kwiatkowski D.J.,
RA Hartwig J.H.;
RT "Human endothelial actin-binding protein (ABP-280, nonmuscle filamin): a
RT molecular leaf spring.";
RL J. Cell Biol. 111:1089-1105(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8088819; DOI=10.1006/geno.1994.1226;
RA Patrosso M.C., Repetto M., Villa A., Milanesi L., Frattini A., Faranda S.,
RA Mancini M., Maestrini E., Toniolo D., Vezzoni P.;
RT "The exon-intron organization of the human X-linked gene (FLN1) encoding
RT actin-binding protein 280.";
RL Genomics 21:71-76(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8733135; DOI=10.1093/hmg/5.5.659;
RA Chen E.Y., Zollo M., Mazzarella R.A., Ciccodicola A., Chen C.-N., Zuo L.,
RA Heiner C., Burough F.W., Ripetto M., Schlessinger D., D'Urso M.;
RT "Long-range sequence analysis in Xq28: thirteen known and six candidate
RT genes in 219.4 kb of high GC DNA between the RCP/GCP and G6PD loci.";
RL Hum. Mol. Genet. 5:659-668(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=20736409; DOI=10.1074/mcp.m110.001719;
RA Li J., Liu F., Wang H., Liu X., Liu J., Li N., Wan F., Wang W., Zhang C.,
RA Jin S., Liu J., Zhu P., Liu Y.;
RT "Systematic mapping and functional analysis of a family of human epididymal
RT secretory sperm-located proteins.";
RL Mol. Cell. Proteomics 9:2517-2528(2010).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Spleen;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=21697133; DOI=10.1167/iovs.11-7479;
RA Oshikawa M., Tsutsui C., Ikegami T., Fuchida Y., Matsubara M., Toyama S.,
RA Usami R., Ohtoko K., Kato S.;
RT "Full-length transcriptome analysis of human retina-derived cell lines
RT ARPE-19 and Y79 using the vector-capping method.";
RL Invest. Ophthalmol. Vis. Sci. 52:6662-6670(2011).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP PROTEIN SEQUENCE OF 2-24; 44-51; 64-87; 101-127; 172-190; 300-376; 384-400;
RP 428-437; 497-504; 581-593; 656-664; 685-700; 761-771; 774-781; 829-837;
RP 842-900; 907-916; 959-973; 983-994; 1020-1032; 1165-1172; 1235-1294;
RP 1297-1312; 1360-1399; 1440-1450; 1465-1486; 1492-1532; 1539-1547;
RP 1550-1592; 1622-1633; 1636-1644; 1726-1753; 1801-1809; 1815-1831;
RP 1892-1907; 1965-1993; 2015-2024; 2026-2049; 2202-2215; 2243-2250;
RP 2265-2289; 2311-2333; 2335-2361; 2396-2405; 2521-2540; 2585-2598 AND
RP 2613-2631, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Platelet;
RA Bienvenut W.V., Claeys D.;
RL Submitted (NOV-2005) to UniProtKB.
RN [10]
RP PROTEIN SEQUENCE OF 25-54; 917-940; 1037-1050; 1754-1783 AND 2148-2168.
RX PubMed=2248958; DOI=10.1021/bi00492a019;
RA Hock R.S., Davis G., Speicher D.W.;
RT "Purification of human smooth muscle filamin and characterization of
RT structural domains and functional sites.";
RL Biochemistry 29:9441-9451(1990).
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1658-1772.
RX PubMed=7689010; DOI=10.1093/hmg/2.6.761;
RA Maestrini E., Patrosso C., Mancini M., Rivella S., Rocchi M., Repetto M.,
RA Villa A., Frattini A., Zoppe M., Vezzoni P., Toniolo D.;
RT "Mapping of two genes encoding isoforms of the actin binding protein ABP-
RT 280, a dystrophin like protein, to Xq28 and to chromosome 7.";
RL Hum. Mol. Genet. 2:761-766(1993).
RN [12]
RP SIMILARITY TO OTHER MEMBERS OF THE FAMILY.
RX PubMed=11153914; DOI=10.1007/s004390000414;
RA Chakarova C., Wehnert M.S., Uhl K., Sakthivel S., Vosberg H.-P.,
RA van der Ven P.F.M., Fuerst D.O.;
RT "Genomic structure and fine mapping of the two human filamin gene
RT paralogues FLNB and FLNC and comparative analysis of the filamin gene
RT family.";
RL Hum. Genet. 107:597-611(2000).
RN [13]
RP INTERACTION WITH PSEN1 AND PSEN2.
RX PubMed=9437013; DOI=10.1523/jneurosci.18-03-00914.1998;
RA Zhang W., Han S.W., McKeel D.W., Goate A., Wu J.Y.;
RT "Interaction of presenilins with the filamin family of actin-binding
RT proteins.";
RL J. Neurosci. 18:914-922(1998).
RN [14]
RP INTERACTION WITH KCND2.
RX PubMed=11102480; DOI=10.1523/jneurosci.20-23-08736.2000;
RA Petrecca K., Miller D.M., Shrier A.;
RT "Localization and enhanced current density of the Kv4.2 potassium channel
RT by interaction with the actin-binding protein filamin.";
RL J. Neurosci. 20:8736-8744(2000).
RN [15]
RP INTERACTION WITH INPPL1.
RX PubMed=11739414; DOI=10.1083/jcb.200104005;
RA Dyson J.M., O'Malley C.J., Becanovic J., Munday A.D., Berndt M.C.,
RA Coghill I.D., Nandurkar H.H., Ooms L.M., Mitchell C.A.;
RT "The SH2-containing inositol polyphosphate 5-phosphatase, SHIP-2, binds
RT filamin and regulates submembraneous actin.";
RL J. Cell Biol. 155:1065-1079(2001).
RN [16]
RP INTERACTION WITH FLNB.
RX PubMed=12393796; DOI=10.1093/hmg/11.23.2845;
RA Sheen V.L., Feng Y., Graham D., Takafuta T., Shapiro S.S., Walsh C.A.;
RT "Filamin A and filamin B are co-expressed within neurons during periods of
RT neuronal migration and can physically interact.";
RL Hum. Mol. Genet. 11:2845-2854(2002).
RN [17]
RP INTERACTION WITH MYOT AND MYOZ1.
RX PubMed=16076904; DOI=10.1242/jcs.02484;
RA Gontier Y., Taivainen A., Fontao L., Sonnenberg A., van der Flier A.,
RA Carpen O., Faulkner G., Borradori L.;
RT "The Z-disc proteins myotilin and FATZ-1 interact with each other and are
RT connected to the sarcolemma via muscle-specific filamins.";
RL J. Cell Sci. 118:3739-3749(2005).
RN [18]
RP REVIEW.
RX PubMed=11336782; DOI=10.1016/s0167-4889(01)00072-6;
RA van der Flier A., Sonnenberg A.;
RT "Structural and functional aspects of filamins.";
RL Biochim. Biophys. Acta 1538:99-117(2001).
RN [19]
RP REVIEW.
RX PubMed=11252955; DOI=10.1038/35052082;
RA Stossel T.P., Condeelis J., Cooley L., Hartwig J.H., Noegel A.,
RA Schleicher M., Shapiro S.S.;
RT "Filamins as integrators of cell mechanics and signalling.";
RL Nat. Rev. Mol. Cell Biol. 2:138-145(2001).
RN [20]
RP INTERACTION WITH CEACAM1, AND SUBCELLULAR LOCATION.
RX PubMed=16291724; DOI=10.1242/jcs.02660;
RA Klaile E., Mueller M.M., Kannicht C., Singer B.B., Lucka L.;
RT "CEACAM1 functionally interacts with filamin A and exerts a dual role in
RT the regulation of cell migration.";
RL J. Cell Sci. 118:5513-5524(2005).
RN [21]
RP INTERACTION WITH FOXC1.
RX PubMed=15684392; DOI=10.1128/mcb.25.4.1415-1424.2005;
RA Berry F.B., O'Neill M.A., Coca-Prados M., Walter M.A.;
RT "FOXC1 transcriptional regulatory activity is impaired by PBX1 in a filamin
RT A-mediated manner.";
RL Mol. Cell. Biol. 25:1415-1424(2005).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1089; SER-1459; SER-2152 AND
RP SER-2284, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [23]
RP INVOLVEMENT IN PVNH1.
RX PubMed=16299064; DOI=10.1136/jmg.2005.038505;
RA Hehr U., Hehr A., Uyanik G., Phelan E., Winkler J., Reardon W.;
RT "A filamin A splice mutation resulting in a syndrome of facial dysmorphism,
RT periventricular nodular heterotopia, and severe constipation reminiscent of
RT cerebro-fronto-facial syndrome.";
RL J. Med. Genet. 43:541-544(2006).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084 AND SER-1459, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [25]
RP INTERACTION WITH ARHGAP24.
RX PubMed=16862148; DOI=10.1038/ncb1437;
RA Ohta Y., Hartwig J.H., Stossel T.P.;
RT "FilGAP, a Rho- and ROCK-regulated GAP for Rac binds filamin A to control
RT actin remodelling.";
RL Nat. Cell Biol. 8:803-814(2006).
RN [26]
RP INVOLVEMENT IN IPOX.
RX PubMed=17357080; DOI=10.1086/513321;
RA Gargiulo A., Auricchio R., Barone M.V., Cotugno G., Reardon W., Milla P.J.,
RA Ballabio A., Ciccodicola A., Auricchio A.;
RT "Filamin A is mutated in X-linked chronic idiopathic intestinal pseudo-
RT obstruction with central nervous system involvement.";
RL Am. J. Hum. Genet. 80:751-758(2007).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [28]
RP INTERACTION WITH ECSCR.
RX PubMed=18556573; DOI=10.1161/atvbaha.108.162511;
RA Armstrong L.-J., Heath V.L., Sanderson S., Kaur S., Beesley J.F.J.,
RA Herbert J.M.J., Legg J.A., Poulsom R., Bicknell R.;
RT "ECSM2, an endothelial specific filamin a binding protein that mediates
RT chemotaxis.";
RL Arterioscler. Thromb. Vasc. Biol. 28:1640-1646(2008).
RN [29]
RP INTERACTION WITH FCGR1A.
RX PubMed=18322202; DOI=10.4049/jimmunol.180.6.3938;
RA Beekman J.M., van der Poel C.E., van der Linden J.A., van den Berg D.L.C.,
RA van den Berghe P.V.E., van de Winkel J.G.J., Leusen J.H.W.;
RT "Filamin A stabilizes FcgammaRI surface expression and prevents its
RT lysosomal routing.";
RL J. Immunol. 180:3938-3945(2008).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1459, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084; SER-1459; SER-2152 AND
RP SER-2158, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1081, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [34]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084; SER-1338; SER-1459;
RP SER-1533; SER-1630; SER-2053; SER-2152; SER-2327; SER-2414 AND SER-2510,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [35]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [36]
RP INTERACTION WITH GP1BA; ITGB7; ITGB2 AND FBLIM1.
RX PubMed=19828450; DOI=10.1074/jbc.m109.060954;
RA Ithychanda S.S., Hsu D., Li H., Yan L., Liu D.D., Liu D., Das M.,
RA Plow E.F., Qin J.;
RT "Identification and characterization of multiple similar ligand-binding
RT repeats in filamin: implication on filamin-mediated receptor clustering and
RT cross-talk.";
RL J. Biol. Chem. 284:35113-35121(2009).
RN [37]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [38]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-508; LYS-700; LYS-781; LYS-837;
RP LYS-2607 AND LYS-2621, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [39]
RP INTERACTION WITH SYK.
RX PubMed=20713593; DOI=10.1084/jem.20100222;
RA Falet H., Pollitt A.Y., Begonja A.J., Weber S.E., Duerschmied D.,
RA Wagner D.D., Watson S.P., Hartwig J.H.;
RT "A novel interaction between FlnA and Syk regulates platelet ITAM-mediated
RT receptor signaling and function.";
RL J. Exp. Med. 207:1967-1979(2010).
RN [40]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1081; SER-1084; SER-1459;
RP SER-1533; SER-1734; SER-2053; SER-2152; SER-2284; SER-2327; THR-2336 AND
RP SER-2414, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [41]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [42]
RP INTERACTION WITH ITGB7 AND FBLIM1, AND DOMAIN.
RX PubMed=21524097; DOI=10.1021/bi2003229;
RA Ithychanda S.S., Qin J.;
RT "Evidence for multisite ligand binding and stretching of filamin by
RT integrin and migfilin.";
RL Biochemistry 50:4229-4231(2011).
RN [43]
RP INTERACTION WITH TAF1B AND MIS18BP1, AND CHARACTERIZATION OF VARIANTS
RP ALA-1159; THR-1188 AND LEU-1199.
RX PubMed=21228480; DOI=10.1271/bbb.100567;
RA Qiu H., Nomiyama R., Moriguchi K., Fukada T., Sugimoto K.;
RT "Identification of novel nuclear protein interactions with the N-terminal
RT part of filamin A.";
RL Biosci. Biotechnol. Biochem. 75:145-147(2011).
RN [44]
RP INVOLVEMENT IN MACROTHROMBOCYTOPENIA, AND VARIANT LYS-1803.
RX PubMed=21960593; DOI=10.1182/blood-2011-07-365601;
RA Nurden P., Debili N., Coupry I., Bryckaert M., Youlyouz-Marfak I., Sole G.,
RA Pons A.C., Berrou E., Adam F., Kauskot A., Lamaziere J.M., Rameau P.,
RA Fergelot P., Rooryck C., Cailley D., Arveiler B., Lacombe D.,
RA Vainchenker W., Nurden A., Goizet C.;
RT "Thrombocytopenia resulting from mutations in filamin A can be expressed as
RT an isolated syndrome.";
RL Blood 118:5928-5937(2011).
RN [45]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-1081; SER-1084;
RP SER-1459; SER-2152 AND SER-2327, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [46]
RP FUNCTION IN CILIOGENESIS, AND INTERACTION WITH TMEM67 AND MKS1.
RX PubMed=22121117; DOI=10.1093/hmg/ddr557;
RA Adams M., Simms R.J., Abdelhamed Z., Dawe H.R., Szymanska K., Logan C.V.,
RA Wheway G., Pitt E., Gull K., Knowles M.A., Blair E., Cross S.H.,
RA Sayer J.A., Johnson C.A.;
RT "A meckelin-filamin A interaction mediates ciliogenesis.";
RL Hum. Mol. Genet. 21:1272-1286(2012).
RN [47]
RP INTERACTION WITH MICALL2.
RX PubMed=23890175; DOI=10.1111/gtc.12078;
RA Sakane A., Alamir Mahmoud Abdallah A., Nakano K., Honda K., Kitamura T.,
RA Imoto I., Matsushita N., Sasaki T.;
RT "Junctional Rab13-binding protein (JRAB) regulates cell spreading via
RT filamins.";
RL Genes Cells 18:810-822(2013).
RN [48]
RP INVOLVEMENT IN CSBSX.
RX PubMed=23037936; DOI=10.1038/gim.2012.123;
RA van der Werf C.S., Sribudiani Y., Verheij J.B., Carroll M., O'Loughlin E.,
RA Chen C.H., Brooks A.S., Liszewski M.K., Atkinson J.P., Hofstra R.M.;
RT "Congenital short bowel syndrome as the presenting symptom in male patients
RT with FLNA mutations.";
RL Genet. Med. 15:310-313(2013).
RN [49]
RP UBIQUITINATION AT LYS-42; LYS-43 AND LYS-135, AND MUTAGENESIS OF LYS-42;
RP LYS-43 AND LYS-135.
RX PubMed=24052262; DOI=10.1074/jbc.m113.496604;
RA Razinia Z., Baldassarre M., Cantelli G., Calderwood D.A.;
RT "ASB2alpha, an E3 ubiquitin ligase specificity subunit, regulates cell
RT spreading and triggers proteasomal degradation of filamins by targeting the
RT filamin calponin homology 1 domain.";
RL J. Biol. Chem. 288:32093-32105(2013).
RN [50]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1081; SER-1084; SER-1301;
RP SER-1459; SER-1533; SER-1630; SER-1835; SER-2128; SER-2152; SER-2158;
RP SER-2284; SER-2327; THR-2336; SER-2338 AND SER-2510, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [51]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1055; SER-1081; SER-1459;
RP SER-1734; SER-1967; SER-2152; SER-2158 AND SER-2163, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [52]
RP FUNCTION, AND INTERACTION WITH CRMP1; DPYSL3 AND DPYSL4.
RX PubMed=25358863; DOI=10.1038/ncomms6325;
RA Nakamura F., Kumeta K., Hida T., Isono T., Nakayama Y.,
RA Kuramata-Matsuoka E., Yamashita N., Uchida Y., Ogura K., Gengyo-Ando K.,
RA Mitani S., Ogino T., Goshima Y.;
RT "Amino- and carboxyl-terminal domains of Filamin-A interact with CRMP1 to
RT mediate Sema3A signalling.";
RL Nat. Commun. 5:5325-5325(2014).
RN [53]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-299, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [54]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-299, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [55]
RP INTERACTION WITH DRD3; MAS1; AGTR1 AND ADRA1D, AND PHOSPHORYLATION AT
RP SER-2152.
RX PubMed=26460884; DOI=10.1021/acs.biochem.5b00975;
RA Tirupula K.C., Ithychanda S.S., Mohan M.L., Naga Prasad S.V., Qin J.,
RA Karnik S.S.;
RT "G Protein-Coupled Receptors Directly Bind Filamin A with High Affinity and
RT Promote Filamin Phosphorylation.";
RL Biochemistry 54:6673-6683(2015).
RN [56]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-299, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [57]
RP PHOSPHORYLATION AT SER-2152 AND THR-2336, REGULATION OF PHOSPHORYLATION AT
RP SER-2152, INTERACTION WITH GP1BA, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25666618; DOI=10.1074/jbc.m114.633446;
RA Ithychanda S.S., Fang X., Mohan M.L., Zhu L., Tirupula K.C.,
RA Naga Prasad S.V., Wang Y.X., Karnik S.S., Qin J.;
RT "A mechanism of global shape-dependent recognition and phosphorylation of
RT filamin by protein kinase A.";
RL J. Biol. Chem. 290:8527-8538(2015).
RN [58]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-299, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [59]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [60]
RP UBIQUITINATION.
RX PubMed=26766444; DOI=10.1016/j.devcel.2015.12.015;
RA Scholz B., Korn C., Wojtarowicz J., Mogler C., Augustin I., Boutros M.,
RA Niehrs C., Augustin H.G.;
RT "Endothelial RSPO3 controls vascular stability and pruning through non-
RT canonical WNT/Ca(2+)/NFAT signaling.";
RL Dev. Cell 36:79-93(2016).
RN [61]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-299, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [62]
RP VARIANT LEU-606.
RX PubMed=30500825; DOI=10.1371/journal.pgen.1007671;
RA Hiatt S.M., Neu M.B., Ramaker R.C., Hardigan A.A., Prokop J.W.,
RA Hancarova M., Prchalova D., Havlovicova M., Prchal J., Stranecky V.,
RA Yim D.K.C., Powis Z., Keren B., Nava C., Mignot C., Rio M.,
RA Revah-Politi A., Hemati P., Stong N., Iglesias A.D., Suchy S.F.,
RA Willaert R., Wentzensen I.M., Wheeler P.G., Brick L., Kozenko M.,
RA Hurst A.C.E., Wheless J.W., Lacassie Y., Myers R.M., Barsh G.S.,
RA Sedlacek Z., Cooper G.M.;
RT "De novo mutations in the GTP/GDP-binding region of RALA, a RAS-like small
RT GTPase, cause intellectual disability and developmental delay.";
RL PLoS Genet. 14:e1007671-e1007671(2018).
RN [63]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2045-2329, AND DOMAIN.
RX PubMed=17690686; DOI=10.1038/sj.emboj.7601827;
RA Lad Y., Kiema T., Jiang P., Pentikainen O.T., Coles C.H., Campbell I.D.,
RA Calderwood D.A., Ylanne J.;
RT "Structure of three tandem filamin domains reveals auto-inhibition of
RT ligand binding.";
RL EMBO J. 26:3993-4004(2007).
RN [64]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 1-278, ACTIN-BINDING REGION, AND
RP SUBUNIT.
RX PubMed=19923718; DOI=10.1107/s0907444909037330;
RA Ruskamo S., Ylanne J.;
RT "Structure of the human filamin A actin-binding domain.";
RL Acta Crystallogr. D 65:1217-1221(2009).
RN [65]
RP STRUCTURE BY NMR OF 1772-1956 AND 1954-2141.
RX PubMed=19622754; DOI=10.1074/jbc.m109.019661;
RA Heikkinen O.K., Ruskamo S., Konarev P.V., Svergun D.I., Iivanainen T.,
RA Heikkinen S.M., Permi P., Koskela H., Kilpelainen I., Ylanne J.;
RT "Atomic structures of two novel immunoglobulin-like domain pairs in the
RT actin cross-linking protein filamin.";
RL J. Biol. Chem. 284:25450-25458(2009).
RN [66]
RP VARIANT PVNH1 PHE-656, AND VARIANT THR-1764.
RX PubMed=11532987; DOI=10.1093/hmg/10.17.1775;
RA Sheen V.L., Dixon P.H., Fox J.W., Hong S.E., Kinton L., Sisodiya S.M.,
RA Duncan J.S., Dubeau F., Scheffer I.E., Schachter S.C., Wilner A.,
RA Henchy R., Crino P., Kamuro K., DiMario F., Berg M., Kuzniecky R.,
RA Cole A.J., Bromfield E., Biber M., Schomer D., Wheless J., Silver K.,
RA Mochida G.H., Berkovic S.F., Andermann F., Andermann E., Dobyns W.B.,
RA Wood N.W., Walsh C.A.;
RT "Mutations in the X-linked filamin 1 gene cause periventricular nodular
RT heterotopia in males as well as in females.";
RL Hum. Mol. Genet. 10:1775-1783(2001).
RN [67]
RP VARIANT MET-528.
RX PubMed=12410386; DOI=10.1007/s00401-002-0594-9;
RA Kakita A., Hayashi S., Moro F., Guerrini R., Ozawa T., Ono K., Kameyama S.,
RA Walsh C.A., Takahashi H.;
RT "Bilateral periventricular nodular heterotopia due to filamin 1 gene
RT mutation: widespread glomeruloid microvascular anomaly and dysplastic
RT cytoarchitecture in the cerebral cortex.";
RL Acta Neuropathol. 104:649-657(2002).
RN [68]
RP VARIANT PVNH1 VAL-82.
RX PubMed=11914408; DOI=10.1212/wnl.58.6.916;
RA Moro F., Carrozzo R., Veggiotti P., Tortorella G., Toniolo D., Volzone A.,
RA Guerrini R.;
RT "Familial periventricular heterotopia: missense and distal truncating
RT mutations of the FLN1 gene.";
RL Neurology 58:916-921(2002).
RN [69]
RP VARIANTS OPD1 PHE-172; TRP-196 AND LEU-207, VARIANTS OPD2 PRO-170; GLY-196;
RP SER-200; LYS-254; PRO-273; LYS-555 AND PHE-1645, VARIANTS FMD1 ALA-1159;
RP LEU-1186 AND ILE-1620 DEL, VARIANTS MNS GLU-1184; THR-1188 AND LEU-1199,
RP AND VARIANTS MET-429 AND THR-1764.
RX PubMed=12612583; DOI=10.1038/ng1119;
RA Robertson S.P., Twigg S.R.F., Sutherland-Smith A.J., Biancalana V.,
RA Gorlin R.J., Horn D., Kenwrick S.J., Kim C.A., Morava E., Newbury-Ecob R.,
RA Oerstavik K.H., Quarrell O.W.J., Schwartz C.E., Shears D.J., Suri M.,
RA Kendrick-Jones J., Wilkie A.O.M.;
RT "Localized mutations in the gene encoding the cytoskeletal protein filamin
RT A cause diverse malformations in humans.";
RL Nat. Genet. 33:487-491(2003).
RN [70]
RP VARIANTS PVNH1 VAL-102 AND PHE-149.
RX PubMed=15249610; DOI=10.1212/01.wnl.0000132818.84827.4d;
RA Guerrini R., Mei D., Sisodiya S.M., Sicca F., Harding B., Takahashi Y.,
RA Dorn T., Yoshida A., Campistol J., Kraemer G., Moro F., Dobyns W.B.,
RA Parrini E.;
RT "Germline and mosaic mutations of FLN1 in men with periventricular
RT heterotopia.";
RL Neurology 63:51-56(2004).
RN [71]
RP VARIANT OTOPALATODIGITAL SPECTRUM DISORDER 1635-ARG--VAL-1637 DEL.
RX PubMed=15654694; DOI=10.1002/ajmg.a.30484;
RA Stefanova M., Meinecke P., Gal A., Bolz H.;
RT "A novel 9 bp deletion in the filamin A gene causes an otopalatodigital-
RT spectrum disorder with a variable, intermediate phenotype.";
RL Am. J. Med. Genet. A 132:386-390(2005).
RN [72]
RP VARIANT OPD1 TYR-203.
RX PubMed=15940695; DOI=10.1002/ajmg.a.30792;
RA Hidalgo-Bravo A., Pompa-Mera E.N., Kofman-Alfaro S., Gonzalez-Bonilla C.R.,
RA Zenteno J.C.;
RT "A novel filamin A D203Y mutation in a female patient with otopalatodigital
RT type 1 syndrome and extremely skewed X chromosome inactivation.";
RL Am. J. Med. Genet. A 136:190-193(2005).
RN [73]
RP VARIANT PVNH1 GLY-39.
RX PubMed=15668422; DOI=10.1212/01.wnl.0000149512.79621.df;
RA Sheen V.L., Jansen A., Chen M.H., Parrini E., Morgan T., Ravenscroft R.,
RA Ganesh V., Underwood T., Wiley J., Leventer R., Vaid R.R., Ruiz D.E.,
RA Hutchins G.M., Menasha J., Willner J., Geng Y., Gripp K.W., Nicholson L.,
RA Berry-Kravis E., Bodell A., Apse K., Hill R.S., Dubeau F., Andermann F.,
RA Barkovich J., Andermann E., Shugart Y.Y., Thomas P., Viri M., Veggiotti P.,
RA Robertson S., Guerrini R., Walsh C.A.;
RT "Filamin A mutations cause periventricular heterotopia with Ehlers-Danlos
RT syndrome.";
RL Neurology 64:254-262(2005).
RN [74]
RP VARIANTS FMD1 LEU-1186 AND CYS-1728.
RX PubMed=16596676; DOI=10.1002/ajmg.a.31213;
RA Zenker M., Naehrlich L., Sticht H., Reis A., Horn D.;
RT "Genotype-epigenotype-phenotype correlations in females with
RT frontometaphyseal dysplasia.";
RL Am. J. Med. Genet. A 140:1069-1073(2006).
RN [75]
RP VARIANT PVNH1 VAL-128.
RX PubMed=15994863; DOI=10.1136/jmg.2004.029173;
RA Gomez-Garre P., Seijo M., Gutierrez-Delicado E., Castro del Rio M.,
RA de la Torre C., Gomez-Abad C., Morales-Corraliza J., Puig M.,
RA Serratosa J.M.;
RT "Ehlers-Danlos syndrome and periventricular nodular heterotopia in a
RT Spanish family with a single FLNA mutation.";
RL J. Med. Genet. 43:232-237(2006).
RN [76]
RP VARIANT OPD2 PHE-210.
RX PubMed=17431908; DOI=10.1002/ajmg.a.31696;
RA Marino-Enriquez A., Lapunzina P., Robertson S.P., Rodriguez J.I.;
RT "Otopalatodigital syndrome type 2 in two siblings with a novel filamin A
RT 629G>T mutation: clinical, pathological, and molecular findings.";
RL Am. J. Med. Genet. A 143:1120-1125(2007).
RN [77]
RP VARIANT FGS2 LEU-1291.
RX PubMed=17632775; DOI=10.1002/ajmg.a.31751;
RA Unger S., Mainberger A., Spitz C., Baehr A., Zeschnigk C., Zabel B.,
RA Superti-Furga A., Morris-Rosendahl D.J.;
RT "Filamin A mutation is one cause of FG syndrome.";
RL Am. J. Med. Genet. A 143:1876-1879(2007).
RN [78]
RP VARIANTS CVD1 ARG-288; GLN-637 AND ASP-711.
RX PubMed=17190868; DOI=10.1161/circulationaha.106.622621;
RA Kyndt F., Gueffet J.P., Probst V., Jaafar P., Legendre A., Le Bouffant F.,
RA Toquet C., Roy E., McGregor L., Lynch S.A., Newbury-Ecob R., Tran V.,
RA Young I., Trochu J.N., Le Marec H., Schott J.J.;
RT "Mutations in the gene encoding filamin A as a cause for familial cardiac
RT valvular dystrophy.";
RL Circulation 115:40-49(2007).
RN [79]
RP VARIANT TOD 1724-VAL--THR-1739 DEL.
RX PubMed=20598277; DOI=10.1016/j.ajhg.2010.06.008;
RA Sun Y., Almomani R., Aten E., Celli J., van der Heijden J., Venselaar H.,
RA Robertson S.P., Baroncini A., Franco B., Basel-Vanagaite L., Horii E.,
RA Drut R., Ariyurek Y., den Dunnen J.T., Breuning M.H.;
RT "Terminal osseous dysplasia is caused by a single recurrent mutation in the
RT FLNA gene.";
RL Am. J. Hum. Genet. 87:146-153(2010).
RN [80]
RP VARIANT MET-528.
RX PubMed=20844545; DOI=10.1038/jhg.2010.114;
RA Kunishima S., Ito-Yamamura Y., Hayakawa A., Yamamoto T., Saito H.;
RT "FLNA p.V528M substitution is neither associated with bilateral
RT periventricular nodular heterotopia nor with macrothrombocytopenia.";
RL J. Hum. Genet. 55:844-846(2010).
RN [81]
RP VARIANTS OPD2 SER-187 AND GLY-196, VARIANTS OPD1 LEU-207; THR-267; ASP-804
RP AND HIS-2391, VARIANTS FMD1 VAL-1142; LEU-1186 AND ARG-1840, AND VARIANTS
RP MNS LEU-1163 AND THR-1188.
RX PubMed=27193221; DOI=10.1038/jhg.2016.37;
RA Moutton S., Fergelot P., Naudion S., Cordier M.P., Sole G., Guerineau E.,
RA Hubert C., Rooryck C., Vuillaume M.L., Houcinat N., Deforges J., Bouron J.,
RA Deves S., Le Merrer M., David A., Genevieve D., Giuliano F., Journel H.,
RA Megarbane A., Faivre L., Chassaing N., Francannet C., Sarrazin E.,
RA Stattin E.L., Vigneron J., Leclair D., Abadie C., Sarda P., Baumann C.,
RA Delrue M.A., Arveiler B., Lacombe D., Goizet C., Coupry I.;
RT "Otopalatodigital spectrum disorders: refinement of the phenotypic and
RT mutational spectrum.";
RL J. Hum. Genet. 61:693-699(2016).
CC -!- FUNCTION: Promotes orthogonal branching of actin filaments and links
CC actin filaments to membrane glycoproteins. Anchors various
CC transmembrane proteins to the actin cytoskeleton and serves as a
CC scaffold for a wide range of cytoplasmic signaling proteins.
CC Interaction with FLNB may allow neuroblast migration from the
CC ventricular zone into the cortical plate. Tethers cell surface-
CC localized furin, modulates its rate of internalization and directs its
CC intracellular trafficking (By similarity). Involved in ciliogenesis.
CC Plays a role in cell-cell contacts and adherens junctions during the
CC development of blood vessels, heart and brain organs. Plays a role in
CC platelets morphology through interaction with SYK that regulates
CC ITAM- and ITAM-like-containing receptor signaling, resulting in by
CC platelet cytoskeleton organization maintenance (By similarity). During
CC the axon guidance process, required for growth cone collapse induced by
CC SEMA3A-mediated stimulation of neurons (PubMed:25358863). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q8BTM8, ECO:0000269|PubMed:22121117,
CC ECO:0000269|PubMed:25358863}.
CC -!- SUBUNIT: Homodimer. Interacts with PDLIM2 (By similarity). Interacts
CC with RFLNA and RFLNB (By similarity). Interacts with FCGR1A, FLNB,
CC FURIN, HSPB7, INPPL1, KCND2, MYOT, MYOZ1, ARHGAP24, PSEN1, PSEN2 and
CC ECSCR. Interacts also with various other binding partners in addition
CC to filamentous actin. Interacts (via N-terminus) with MIS18BP1 (via N-
CC terminus). Interacts (via N-terminus) with TAF1B. Interacts with TMEM67
CC (via C-terminus) and MKS1. Interacts (via actin-binding domain) with
CC MICALL2 (via CH domain). Interacts (via filamin repeat 5) with SYK;
CC docks SYK to the plasma membrane (PubMed:20713593). Interacts (via
CC filamin repeats 19 and 21) with DRD3; increased PKA-mediated
CC phosphorylation at Ser-2152. Interacts (via filamin repeat 21) with
CC MAS1, AGTR1 and ADRA1D; increases PKA-mediated phosphorylation of FLNA
CC at Ser-2152 (PubMed:26460884). Interacts (via filamin repeats 4, 9, 12,
CC 17, 19, 21, and 23) with GP1BA (high affinity), ITGB7, ITGB2 and FBLIM1
CC (PubMed:19828450, PubMed:21524097, PubMed:25666618). Interacts with
CC CEACAM1 (via cytoplasmic domain); inhibits cell migration and cell
CC scattering by interfering with the interaction between FLNA and RALA
CC (PubMed:16291724). Interacts with FOXC1 (PubMed:15684392). Interacts
CC (via calponin-homology (CH) domain 1 and filamin repeat 24) with CRMP1;
CC the interaction alters FLNA ternary structure and thus promotes FLNA
CC dissociation from F-actin (PubMed:25358863). Interacts with
CC DPYSL3/CRMP3 and DPYSL4/CRMP4 (PubMed:25358863). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q8BTM8, ECO:0000269|PubMed:11102480,
CC ECO:0000269|PubMed:11739414, ECO:0000269|PubMed:12393796,
CC ECO:0000269|PubMed:15684392, ECO:0000269|PubMed:16076904,
CC ECO:0000269|PubMed:16291724, ECO:0000269|PubMed:16862148,
CC ECO:0000269|PubMed:18322202, ECO:0000269|PubMed:18556573,
CC ECO:0000269|PubMed:19828450, ECO:0000269|PubMed:19923718,
CC ECO:0000269|PubMed:20713593, ECO:0000269|PubMed:21228480,
CC ECO:0000269|PubMed:21524097, ECO:0000269|PubMed:22121117,
CC ECO:0000269|PubMed:23890175, ECO:0000269|PubMed:25358863,
CC ECO:0000269|PubMed:25666618, ECO:0000269|PubMed:26460884,
CC ECO:0000269|PubMed:9437013}.
CC -!- INTERACTION:
CC P21333; Q8N264: ARHGAP24; NbExp=6; IntAct=EBI-350432, EBI-988764;
CC P21333; O95067: CCNB2; NbExp=8; IntAct=EBI-350432, EBI-375024;
CC P21333; P46108: CRK; NbExp=3; IntAct=EBI-350432, EBI-886;
CC P21333; O75369: FLNB; NbExp=5; IntAct=EBI-350432, EBI-352089;
CC P21333; Q12948: FOXC1; NbExp=8; IntAct=EBI-350432, EBI-1175253;
CC P21333; P51114: FXR1; NbExp=2; IntAct=EBI-350432, EBI-713291;
CC P21333; P62993: GRB2; NbExp=2; IntAct=EBI-350432, EBI-401755;
CC P21333; P08514-1: ITGA2B; NbExp=3; IntAct=EBI-350432, EBI-15805658;
CC P21333; P05556: ITGB1; NbExp=5; IntAct=EBI-350432, EBI-703066;
CC P21333; P05106: ITGB3; NbExp=3; IntAct=EBI-350432, EBI-702847;
CC P21333; P26010: ITGB7; NbExp=6; IntAct=EBI-350432, EBI-702932;
CC P21333; P26010-1: ITGB7; NbExp=2; IntAct=EBI-350432, EBI-15944630;
CC P21333; O14786: NRP1; NbExp=2; IntAct=EBI-350432, EBI-1187100;
CC P21333; P35372: OPRM1; NbExp=5; IntAct=EBI-350432, EBI-2624570;
CC P21333; Q86SQ0: PHLDB2; NbExp=3; IntAct=EBI-350432, EBI-2798483;
CC P21333; Q9BYB0: SHANK3; NbExp=2; IntAct=EBI-350432, EBI-1752330;
CC P21333; P07228: ITGB1; Xeno; NbExp=2; IntAct=EBI-350432, EBI-5606437;
CC P21333; PRO_0000037548 [Q9WMX2]; Xeno; NbExp=6; IntAct=EBI-350432, EBI-6863741;
CC P21333; PRO_0000037551 [Q9WMX2]; Xeno; NbExp=6; IntAct=EBI-350432, EBI-6863748;
CC P21333-2; Q6UY14-3: ADAMTSL4; NbExp=6; IntAct=EBI-9641086, EBI-10173507;
CC P21333-2; P05067: APP; NbExp=3; IntAct=EBI-9641086, EBI-77613;
CC P21333-2; Q14457: BECN1; NbExp=3; IntAct=EBI-9641086, EBI-949378;
CC P21333-2; Q96IK1-2: BOD1; NbExp=3; IntAct=EBI-9641086, EBI-18924329;
CC P21333-2; Q9BSJ5: C17orf80; NbExp=3; IntAct=EBI-9641086, EBI-2872520;
CC P21333-2; Q96NX5: CAMK1G; NbExp=3; IntAct=EBI-9641086, EBI-3920838;
CC P21333-2; Q8N5S9-2: CAMKK1; NbExp=3; IntAct=EBI-9641086, EBI-25850646;
CC P21333-2; Q6ZP82: CCDC141; NbExp=3; IntAct=EBI-9641086, EBI-928795;
CC P21333-2; Q8IUI8: CRLF3; NbExp=3; IntAct=EBI-9641086, EBI-2872414;
CC P21333-2; P53672: CRYBA2; NbExp=3; IntAct=EBI-9641086, EBI-750444;
CC P21333-2; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-9641086, EBI-3867333;
CC P21333-2; Q96D03: DDIT4L; NbExp=5; IntAct=EBI-9641086, EBI-742054;
CC P21333-2; O00472: ELL2; NbExp=3; IntAct=EBI-9641086, EBI-395274;
CC P21333-2; P07148: FABP1; NbExp=3; IntAct=EBI-9641086, EBI-2115989;
CC P21333-2; Q6P1L5: FAM117B; NbExp=3; IntAct=EBI-9641086, EBI-3893327;
CC P21333-2; Q8TAK5: GABPB2; NbExp=3; IntAct=EBI-9641086, EBI-8468945;
CC P21333-2; F2Z2M7: GALNT10; NbExp=3; IntAct=EBI-9641086, EBI-23893155;
CC P21333-2; Q9Y4H4: GPSM3; NbExp=3; IntAct=EBI-9641086, EBI-347538;
CC P21333-2; Q9XRX5-2: HHLA3; NbExp=3; IntAct=EBI-9641086, EBI-12051311;
CC P21333-2; P17066: HSPA6; NbExp=3; IntAct=EBI-9641086, EBI-355106;
CC P21333-2; Q9UBY9: HSPB7; NbExp=10; IntAct=EBI-9641086, EBI-739361;
CC P21333-2; P80217-2: IFI35; NbExp=3; IntAct=EBI-9641086, EBI-12823003;
CC P21333-2; Q9UKP3-2: ITGB1BP2; NbExp=3; IntAct=EBI-9641086, EBI-25856470;
CC P21333-2; Q8WZ19: KCTD13; NbExp=3; IntAct=EBI-9641086, EBI-742916;
CC P21333-2; Q8N5Z5: KCTD17; NbExp=3; IntAct=EBI-9641086, EBI-743960;
CC P21333-2; Q53G59: KLHL12; NbExp=6; IntAct=EBI-9641086, EBI-740929;
CC P21333-2; Q8TCE9: LGALS14; NbExp=6; IntAct=EBI-9641086, EBI-10274069;
CC P21333-2; Q14693: LPIN1; NbExp=3; IntAct=EBI-9641086, EBI-5278370;
CC P21333-2; Q8TD91-2: MAGEC3; NbExp=3; IntAct=EBI-9641086, EBI-10694180;
CC P21333-2; P02795: MT2A; NbExp=3; IntAct=EBI-9641086, EBI-996616;
CC P21333-2; Q9NP98: MYOZ1; NbExp=6; IntAct=EBI-9641086, EBI-744402;
CC P21333-2; Q9NQS3: NECTIN3; NbExp=3; IntAct=EBI-9641086, EBI-2826725;
CC P21333-2; Q9BRX2: PELO; NbExp=6; IntAct=EBI-9641086, EBI-1043580;
CC P21333-2; Q8TCD6: PHOSPHO2; NbExp=3; IntAct=EBI-9641086, EBI-2861380;
CC P21333-2; Q9H8W4: PLEKHF2; NbExp=5; IntAct=EBI-9641086, EBI-742388;
CC P21333-2; O43741: PRKAB2; NbExp=3; IntAct=EBI-9641086, EBI-1053424;
CC P21333-2; Q09028: RBBP4; NbExp=3; IntAct=EBI-9641086, EBI-620823;
CC P21333-2; P57052: RBM11; NbExp=3; IntAct=EBI-9641086, EBI-741332;
CC P21333-2; Q04864: REL; NbExp=3; IntAct=EBI-9641086, EBI-307352;
CC P21333-2; Q6ZTI6: RFLNA; NbExp=3; IntAct=EBI-9641086, EBI-10200920;
CC P21333-2; Q6ZTI6-2: RFLNA; NbExp=3; IntAct=EBI-9641086, EBI-12362431;
CC P21333-2; Q8N488: RYBP; NbExp=3; IntAct=EBI-9641086, EBI-752324;
CC P21333-2; O15127: SCAMP2; NbExp=3; IntAct=EBI-9641086, EBI-712703;
CC P21333-2; P08195-4: SLC3A2; NbExp=3; IntAct=EBI-9641086, EBI-12832276;
CC P21333-2; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-9641086, EBI-358489;
CC P21333-2; Q13573: SNW1; NbExp=3; IntAct=EBI-9641086, EBI-632715;
CC P21333-2; Q9BXN6: SPANXD; NbExp=3; IntAct=EBI-9641086, EBI-10301202;
CC P21333-2; P15884: TCF4; NbExp=3; IntAct=EBI-9641086, EBI-533224;
CC P21333-2; P04637: TP53; NbExp=3; IntAct=EBI-9641086, EBI-366083;
CC P21333-2; Q9NX94: WBP1L; NbExp=3; IntAct=EBI-9641086, EBI-10316321;
CC P21333-2; Q9BRX9: WDR83; NbExp=3; IntAct=EBI-9641086, EBI-7705033;
CC P21333-2; O95789-4: ZMYM6; NbExp=3; IntAct=EBI-9641086, EBI-12949277;
CC P21333-2; Q96E88; NbExp=3; IntAct=EBI-9641086, EBI-10976904;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:16291724}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q8BTM8}. Perikaryon
CC {ECO:0000250|UniProtKB:Q8BTM8}. Cell projection, growth cone
CC {ECO:0000250|UniProtKB:Q8BTM8}. Note=Colocalizes with CPMR1 in the
CC central region of DRG neuron growth cone (By similarity). Following
CC SEMA3A stimulation of DRG neurons, colocalizes with F-actin (By
CC similarity). {ECO:0000250|UniProtKB:Q8BTM8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P21333-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P21333-2; Sequence=VSP_035454;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: Comprised of a NH2-terminal actin-binding domain, 24
CC immunoglobulin-like internally homologous repeats and two hinge
CC regions. Repeat 24 and the second hinge domain are important for dimer
CC formation. Filamin repeat 20 interacts with filamin repeat 21 masking
CC the ligand binding site on filamin repeat 21, resulting in an
CC autoinhibited conformation (PubMed:17690686). The autoinhibition can be
CC relieved by ligands like ITGB7 or FBLIM1 (PubMed:21524097). Filamin
CC repeats 19 and 21 can simultaneously engage ligands (PubMed:21524097).
CC {ECO:0000269|PubMed:17690686, ECO:0000269|PubMed:21524097}.
CC -!- PTM: Phosphorylation at Ser-2152 is negatively regulated by the
CC autoinhibited conformation of filamin repeats 19-21. Ligand binding
CC induces a conformational switch triggering phosphorylation at Ser-2152
CC by PKA. {ECO:0000269|PubMed:25666618}.
CC -!- PTM: Phosphorylation extent changes in response to cell activation.
CC -!- PTM: Polyubiquitination in the CH1 domain by a SCF-like complex
CC containing ASB2 leads to proteasomal degradation. Prior dissociation
CC from actin may be required to expose the target lysines
CC (PubMed:24052262). Ubiquitinated in endothelial cells by RNF213
CC downstream of the non-canonical Wnt signaling pathway, leading to its
CC degradation by the proteasome (PubMed:26766444).
CC {ECO:0000269|PubMed:24052262, ECO:0000269|PubMed:26766444}.
CC -!- DISEASE: Periventricular nodular heterotopia 1 (PVNH1) [MIM:300049]: A
CC developmental disorder characterized by the presence of periventricular
CC nodules of cerebral gray matter, resulting from a failure of neurons to
CC migrate normally from the lateral ventricular proliferative zone, where
CC they are formed, to the cerebral cortex. PVNH1 is an X-linked dominant
CC form. Heterozygous females have normal intelligence but suffer from
CC seizures and various manifestations outside the central nervous system,
CC especially related to the vascular system. Hemizygous affected males
CC die in the prenatal or perinatal period. {ECO:0000269|PubMed:11532987,
CC ECO:0000269|PubMed:11914408, ECO:0000269|PubMed:15249610,
CC ECO:0000269|PubMed:15668422, ECO:0000269|PubMed:15994863,
CC ECO:0000269|PubMed:16299064}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Otopalatodigital syndrome 1 (OPD1) [MIM:311300]: X-linked
CC dominant multiple congenital anomalies disease mainly characterized by
CC a generalized skeletal dysplasia, mild intellectual disability, hearing
CC loss, cleft palate, and typical facial anomalies. OPD1 belongs to a
CC group of X-linked skeletal dysplasias known as oto-palato-digital
CC syndrome spectrum disorders that also include OPD2, Melnick-Needles
CC syndrome (MNS), and frontometaphyseal dysplasia (FMD). Remodeling of
CC the cytoskeleton is central to the modulation of cell shape and
CC migration. FLNA is a widely expressed protein that regulates re-
CC organization of the actin cytoskeleton by interacting with integrins,
CC transmembrane receptor complexes and second messengers. Males with OPD1
CC have cleft palate, malformations of the ossicles causing deafness and
CC milder bone and limb defects than those associated with OPD2. Obligate
CC female carriers of mutations causing both OPD1 and OPD2 have variable
CC (often milder) expression of a similar phenotypic spectrum.
CC {ECO:0000269|PubMed:12612583, ECO:0000269|PubMed:15940695,
CC ECO:0000269|PubMed:27193221}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Otopalatodigital syndrome 2 (OPD2) [MIM:304120]: Congenital
CC bone disorder that is characterized by abnormally modeled, bowed bones,
CC small or absent first digits and, more variably, cleft palate,
CC posterior fossa brain anomalies, omphalocele and cardiac defects.
CC {ECO:0000269|PubMed:12612583, ECO:0000269|PubMed:17431908,
CC ECO:0000269|PubMed:27193221}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Frontometaphyseal dysplasia 1 (FMD1) [MIM:305620]: An X-linked
CC disease characterized by generalized skeletal dysplasia, deafness, and
CC urogenital defects. {ECO:0000269|PubMed:12612583,
CC ECO:0000269|PubMed:16596676, ECO:0000269|PubMed:27193221}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Melnick-Needles syndrome (MNS) [MIM:309350]: Severe congenital
CC bone disorder characterized by typical facies (exophthalmos, full
CC cheeks, micrognathia and malalignment of teeth), flaring of the
CC metaphyses of long bones, s-like curvature of bones of legs, irregular
CC constrictions in the ribs, and sclerosis of base of skull.
CC {ECO:0000269|PubMed:12612583, ECO:0000269|PubMed:27193221}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Intestinal pseudoobstruction, neuronal, chronic idiopathic, X-
CC linked (IPOX) [MIM:300048]: A disease characterized by a severe
CC abnormality of gastrointestinal motility due to primary qualitative
CC defects of enteric ganglia and nerve fibers. Affected individuals
CC manifest recurrent signs of intestinal obstruction in the absence of
CC any mechanical lesion. {ECO:0000269|PubMed:17357080}. Note=The disease
CC is caused by variants affecting the gene represented in this entry.
CC -!- DISEASE: FG syndrome 2 (FGS2) [MIM:300321]: FG syndrome (FGS) is an X-
CC linked disorder characterized by intellectual disability, relative
CC macrocephaly, hypotonia and constipation.
CC {ECO:0000269|PubMed:17632775}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Terminal osseous dysplasia (TOD) [MIM:300244]: A rare X-linked
CC dominant male-lethal disease characterized by skeletal dysplasia of the
CC limbs, pigmentary defects of the skin and recurrent digital fibroma
CC during infancy. A significant phenotypic variability is observed in
CC affected females. {ECO:0000269|PubMed:20598277}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- DISEASE: Cardiac valvular dysplasia, X-linked (CVD1) [MIM:314400]: A
CC rare X-linked heart disease characterized by mitral and/or aortic valve
CC regurgitation. The histologic features include fragmentation of
CC collagenous bundles within the valve fibrosa and accumulation of
CC proteoglycans, which produces excessive valve tissue leading to
CC billowing of the valve leaflets. {ECO:0000269|PubMed:17190868}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- DISEASE: Note=Defects in FLNA may be a cause of macrothrombocytopenia,
CC a disorder characterized by subnormal levels of blood platelets. Blood
CC platelets are abnormally enlarged (PubMed:21960593).
CC {ECO:0000269|PubMed:21960593}.
CC -!- DISEASE: Congenital short bowel syndrome, X-linked (CSBSX)
CC [MIM:300048]: A disease characterized by a shortened small intestine,
CC and malabsorption. The mean length of the small intestine in affected
CC individuals is approximately 50 cm, compared with a normal length at
CC birth of 190-280 cm. It is associated with significant mortality and
CC morbidity. Infants usually present with failure to thrive, recurrent
CC vomiting, and diarrhea. {ECO:0000269|PubMed:23037936}. Note=The disease
CC is caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the filamin family. {ECO:0000305}.
CC -!- CAUTION: Variant Thr-1764 has been originally associated with
CC periventricular nodular heterotopia. It has been subsequently reported
CC as a benign polymorphism. {ECO:0000305|PubMed:12612583}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC03408.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X53416; CAA37495.1; -; mRNA.
DR EMBL; L44140; AAA92644.1; -; Genomic_DNA.
DR EMBL; X70082; CAA49687.1; -; Genomic_DNA.
DR EMBL; X70085; CAA49690.1; -; Genomic_DNA.
DR EMBL; GU727643; ADU87644.1; -; mRNA.
DR EMBL; AK090427; BAC03408.2; ALT_INIT; mRNA.
DR EMBL; AB593010; BAJ83965.1; -; mRNA.
DR EMBL; BX664723; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX936346; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471172; EAW72745.1; -; Genomic_DNA.
DR EMBL; CH471172; EAW72746.1; -; Genomic_DNA.
DR CCDS; CCDS44021.1; -. [P21333-2]
DR CCDS; CCDS48194.1; -. [P21333-1]
DR PIR; A37098; A37098.
DR RefSeq; NP_001104026.1; NM_001110556.1. [P21333-1]
DR RefSeq; NP_001447.2; NM_001456.3. [P21333-2]
DR PDB; 2AAV; NMR; -; A=1863-1956.
DR PDB; 2BP3; X-ray; 2.32 A; A/B=1863-1956.
DR PDB; 2BRQ; X-ray; 2.10 A; A/B=2236-2329.
DR PDB; 2J3S; X-ray; 2.50 A; A/B=2045-2329.
DR PDB; 2JF1; X-ray; 2.20 A; A=2236-2329.
DR PDB; 2K3T; NMR; -; A=2427-2522.
DR PDB; 2K7P; NMR; -; A=1772-1956.
DR PDB; 2K7Q; NMR; -; A=1954-2141.
DR PDB; 2MTP; NMR; -; A=2236-2330.
DR PDB; 2W0P; X-ray; 1.90 A; A/B=2236-2329.
DR PDB; 2WFN; X-ray; 3.20 A; A/B=1-278.
DR PDB; 3CNK; X-ray; 1.65 A; A/B=2559-2647.
DR PDB; 3HOC; X-ray; 2.30 A; A/B=2-269.
DR PDB; 3HOP; X-ray; 2.30 A; A/B=2-269.
DR PDB; 3HOR; X-ray; 2.70 A; A/B=2-269.
DR PDB; 3ISW; X-ray; 2.80 A; A/B=2236-2329.
DR PDB; 3RGH; X-ray; 2.44 A; A/B=1158-1252.
DR PDB; 4M9P; X-ray; 1.72 A; A=478-766.
DR PDB; 4P3W; X-ray; 2.00 A; A/B/C/D/E/F=2152-2329.
DR PDB; 5XR1; NMR; -; A=2236-2329.
DR PDB; 6D8C; EM; 3.54 A; A/B/C/D/E=1-278.
DR PDB; 6EW1; X-ray; 2.31 A; A=478-766.
DR PDBsum; 2AAV; -.
DR PDBsum; 2BP3; -.
DR PDBsum; 2BRQ; -.
DR PDBsum; 2J3S; -.
DR PDBsum; 2JF1; -.
DR PDBsum; 2K3T; -.
DR PDBsum; 2K7P; -.
DR PDBsum; 2K7Q; -.
DR PDBsum; 2MTP; -.
DR PDBsum; 2W0P; -.
DR PDBsum; 2WFN; -.
DR PDBsum; 3CNK; -.
DR PDBsum; 3HOC; -.
DR PDBsum; 3HOP; -.
DR PDBsum; 3HOR; -.
DR PDBsum; 3ISW; -.
DR PDBsum; 3RGH; -.
DR PDBsum; 4M9P; -.
DR PDBsum; 4P3W; -.
DR PDBsum; 5XR1; -.
DR PDBsum; 6D8C; -.
DR PDBsum; 6EW1; -.
DR AlphaFoldDB; P21333; -.
DR SASBDB; P21333; -.
DR SMR; P21333; -.
DR BioGRID; 108605; 436.
DR ComplexPortal; CPX-117; Glycoprotein Ib-IX-V-Filamin-A complex.
DR ComplexPortal; CPX-122; Filamin A homodimer.
DR CORUM; P21333; -.
DR DIP; DIP-1136N; -.
DR IntAct; P21333; 319.
DR MINT; P21333; -.
DR STRING; 9606.ENSP00000358866; -.
DR DrugBank; DB11638; Artenimol.
DR MoonDB; P21333; Predicted.
DR TCDB; 8.A.66.1.4; the dystrophin (dystrophin) family.
DR CarbonylDB; P21333; -.
DR GlyGen; P21333; 4 sites, 2 O-linked glycans (4 sites).
DR iPTMnet; P21333; -.
DR MetOSite; P21333; -.
DR PhosphoSitePlus; P21333; -.
DR SwissPalm; P21333; -.
DR BioMuta; FLNA; -.
DR DMDM; 116241365; -.
DR OGP; P21333; -.
DR CPTAC; CPTAC-508; -.
DR CPTAC; CPTAC-509; -.
DR EPD; P21333; -.
DR jPOST; P21333; -.
DR MassIVE; P21333; -.
DR MaxQB; P21333; -.
DR PaxDb; P21333; -.
DR PeptideAtlas; P21333; -.
DR PRIDE; P21333; -.
DR ProteomicsDB; 53859; -. [P21333-1]
DR ProteomicsDB; 53860; -. [P21333-2]
DR ABCD; P21333; 3 sequenced antibodies.
DR Antibodypedia; 341; 691 antibodies from 39 providers.
DR DNASU; 2316; -.
DR Ensembl; ENST00000360319.9; ENSP00000353467.4; ENSG00000196924.19. [P21333-2]
DR Ensembl; ENST00000369850.10; ENSP00000358866.3; ENSG00000196924.19. [P21333-1]
DR GeneID; 2316; -.
DR KEGG; hsa:2316; -.
DR MANE-Select; ENST00000369850.10; ENSP00000358866.3; NM_001110556.2; NP_001104026.1.
DR UCSC; uc004fkk.3; human. [P21333-1]
DR CTD; 2316; -.
DR DisGeNET; 2316; -.
DR GeneCards; FLNA; -.
DR GeneReviews; FLNA; -.
DR HGNC; HGNC:3754; FLNA.
DR HPA; ENSG00000196924; Tissue enhanced (endometrium).
DR MalaCards; FLNA; -.
DR MIM; 300017; gene.
DR MIM; 300048; phenotype.
DR MIM; 300049; phenotype.
DR MIM; 300244; phenotype.
DR MIM; 300321; phenotype.
DR MIM; 304120; phenotype.
DR MIM; 305620; phenotype.
DR MIM; 309350; phenotype.
DR MIM; 311300; phenotype.
DR MIM; 314400; phenotype.
DR neXtProt; NX_P21333; -.
DR OpenTargets; ENSG00000196924; -.
DR Orphanet; 2301; Congenital short bowel syndrome.
DR Orphanet; 555877; FLNA-related X-linked myxomatous valvular dysplasia.
DR Orphanet; 1826; Frontometaphyseal dysplasia.
DR Orphanet; 2484; Melnick-Needles syndrome.
DR Orphanet; 99811; Neuronal intestinal pseudoobstruction.
DR Orphanet; 323; NON RARE IN EUROPE: FG syndrome phenotypic spectrum.
DR Orphanet; 90650; Otopalatodigital syndrome type 1.
DR Orphanet; 90652; Otopalatodigital syndrome type 2.
DR Orphanet; 98892; Periventricular nodular heterotopia.
DR Orphanet; 88630; Terminal osseous dysplasia-pigmentary defects syndrome.
DR Orphanet; 75497; X-linked Ehlers-Danlos syndrome.
DR Orphanet; 482606; X-linked keloid scarring-reduced joint mobility-increased optic cup-to-disc ratio syndrome.
DR PharmGKB; PA28172; -.
DR VEuPathDB; HostDB:ENSG00000196924; -.
DR eggNOG; KOG0518; Eukaryota.
DR GeneTree; ENSGT00940000153588; -.
DR InParanoid; P21333; -.
DR OMA; IPMTPFR; -.
DR OrthoDB; 437627at2759; -.
DR PhylomeDB; P21333; -.
DR TreeFam; TF313685; -.
DR PathwayCommons; P21333; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR Reactome; R-HSA-430116; GP1b-IX-V activation signalling.
DR Reactome; R-HSA-446353; Cell-extracellular matrix interactions.
DR Reactome; R-HSA-5627123; RHO GTPases activate PAKs.
DR Reactome; R-HSA-8983711; OAS antiviral response.
DR SignaLink; P21333; -.
DR SIGNOR; P21333; -.
DR BioGRID-ORCS; 2316; 13 hits in 709 CRISPR screens.
DR ChiTaRS; FLNA; human.
DR EvolutionaryTrace; P21333; -.
DR GeneWiki; FLNA; -.
DR GenomeRNAi; 2316; -.
DR Pharos; P21333; Tbio.
DR PRO; PR:P21333; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P21333; protein.
DR Bgee; ENSG00000196924; Expressed in right coronary artery and 198 other tissues.
DR ExpressionAtlas; P21333; baseline and differential.
DR Genevisible; P21333; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:WormBase.
DR GO; GO:0032432; C:actin filament bundle; IEA:Ensembl.
DR GO; GO:0044295; C:axonal growth cone; IEA:Ensembl.
DR GO; GO:0005903; C:brush border; IEA:Ensembl.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:1990779; C:glycoprotein Ib-IX-V complex; IC:ComplexPortal.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0031523; C:Myb complex; IDA:MGI.
DR GO; GO:0005730; C:nucleolus; IMP:CACAO.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl.
DR GO; GO:0030018; C:Z disc; ISS:BHF-UCL.
DR GO; GO:0051015; F:actin filament binding; IDA:BHF-UCL.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0034988; F:Fc-gamma receptor I complex binding; IDA:BHF-UCL.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IPI:UniProtKB.
DR GO; GO:0051020; F:GTPase binding; IPI:UniProtKB.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0015459; F:potassium channel regulator activity; IDA:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL.
DR GO; GO:0005080; F:protein kinase C binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IDA:BHF-UCL.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL.
DR GO; GO:0051764; P:actin crosslink formation; IDA:BHF-UCL.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IDA:BHF-UCL.
DR GO; GO:0007195; P:adenylate cyclase-inhibiting dopamine receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR GO; GO:0007597; P:blood coagulation, intrinsic pathway; IC:ComplexPortal.
DR GO; GO:0001974; P:blood vessel remodeling; IEA:Ensembl.
DR GO; GO:0045216; P:cell-cell junction organization; IEA:Ensembl.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0051220; P:cytoplasmic sequestering of protein; IMP:BHF-UCL.
DR GO; GO:0045022; P:early endosome to late endosome transport; IEA:Ensembl.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; IEA:Ensembl.
DR GO; GO:0045184; P:establishment of protein localization; IDA:BHF-UCL.
DR GO; GO:0003007; P:heart morphogenesis; IEA:Ensembl.
DR GO; GO:0035855; P:megakaryocyte development; IC:ComplexPortal.
DR GO; GO:0090307; P:mitotic spindle assembly; IDA:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:CACAO.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IEA:Ensembl.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; IMP:BHF-UCL.
DR GO; GO:0016479; P:negative regulation of transcription by RNA polymerase I; IDA:CACAO.
DR GO; GO:0070527; P:platelet aggregation; HMP:UniProtKB.
DR GO; GO:0048680; P:positive regulation of axon regeneration; IEA:Ensembl.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; HMP:UniProtKB.
DR GO; GO:2001046; P:positive regulation of integrin-mediated signaling pathway; IMP:CACAO.
DR GO; GO:0010572; P:positive regulation of platelet activation; IC:ComplexPortal.
DR GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; IDA:BHF-UCL.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IMP:UniProtKB.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IMP:CACAO.
DR GO; GO:0034394; P:protein localization to cell surface; IDA:BHF-UCL.
DR GO; GO:0072659; P:protein localization to plasma membrane; IDA:BHF-UCL.
DR GO; GO:0050821; P:protein stabilization; IMP:BHF-UCL.
DR GO; GO:0043113; P:receptor clustering; IDA:BHF-UCL.
DR GO; GO:0032231; P:regulation of actin filament bundle assembly; IEA:Ensembl.
DR GO; GO:0030334; P:regulation of cell migration; IDA:UniProtKB.
DR GO; GO:1905000; P:regulation of membrane repolarization during atrial cardiac muscle cell action potential; IC:BHF-UCL.
DR GO; GO:1905031; P:regulation of membrane repolarization during cardiac muscle cell action potential; ISS:BHF-UCL.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IC:ComplexPortal.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; IGI:WormBase.
DR GO; GO:0050808; P:synapse organization; IEA:Ensembl.
DR GO; GO:0090042; P:tubulin deacetylation; IMP:CACAO.
DR GO; GO:0044319; P:wound healing, spreading of cells; IDA:UniProtKB.
DR CDD; cd00014; CH; 2.
DR DisProt; DP01950; -.
DR Gene3D; 1.10.418.10; -; 2.
DR Gene3D; 2.60.40.10; -; 24.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR044801; Filamin.
DR InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR InterPro; IPR001298; Filamin/ABP280_rpt.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR38537; PTHR38537; 1.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF00630; Filamin; 23.
DR SMART; SM00033; CH; 2.
DR SMART; SM00557; IG_FLMN; 24.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF81296; SSF81296; 24.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
DR PROSITE; PS50194; FILAMIN_REPEAT; 24.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Alternative splicing;
KW Cell projection; Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton;
KW Deafness; Direct protein sequencing; Disease variant; Isopeptide bond;
KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 2..2647
FT /note="Filamin-A"
FT /id="PRO_0000087296"
FT DOMAIN 43..149
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 166..269
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 276..374
FT /note="Filamin 1"
FT REPEAT 376..474
FT /note="Filamin 2"
FT REPEAT 475..570
FT /note="Filamin 3"
FT REPEAT 571..663
FT /note="Filamin 4"
FT REPEAT 667..763
FT /note="Filamin 5"
FT REPEAT 764..866
FT /note="Filamin 6"
FT REPEAT 867..965
FT /note="Filamin 7"
FT REPEAT 966..1061
FT /note="Filamin 8"
FT REPEAT 1062..1154
FT /note="Filamin 9"
FT REPEAT 1155..1249
FT /note="Filamin 10"
FT REPEAT 1250..1349
FT /note="Filamin 11"
FT REPEAT 1350..1442
FT /note="Filamin 12"
FT REPEAT 1443..1539
FT /note="Filamin 13"
FT REPEAT 1540..1636
FT /note="Filamin 14"
FT REPEAT 1649..1740
FT /note="Filamin 15"
FT REPEAT 1779..1860
FT /note="Filamin 16"
FT REPEAT 1861..1950
FT /note="Filamin 17"
FT REPEAT 1951..2039
FT /note="Filamin 18"
FT REPEAT 2042..2131
FT /note="Filamin 19"
FT REPEAT 2132..2230
FT /note="Filamin 20"
FT REPEAT 2233..2325
FT /note="Filamin 21"
FT REPEAT 2327..2420
FT /note="Filamin 22"
FT REPEAT 2424..2516
FT /note="Filamin 23"
FT REPEAT 2552..2646
FT /note="Filamin 24"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..274
FT /note="Actin-binding"
FT REGION 271..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1361..1382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1490..1607
FT /note="Interaction with furin"
FT /evidence="ECO:0000250"
FT REGION 1741..1778
FT /note="Hinge 1"
FT REGION 2517..2647
FT /note="Self-association site, tail"
FT REGION 2517..2551
FT /note="Hinge 2"
FT COMPBIAS 1363..1378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 1761..1762
FT /note="Cleavage; by calpain"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:25944712"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 376
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BTM8"
FT MOD_RES 508
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 700
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 781
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 837
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 865
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BTM8"
FT MOD_RES 906
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BTM8"
FT MOD_RES 968
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BTM8"
FT MOD_RES 1055
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1071
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BTM8"
FT MOD_RES 1071
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BTM8"
FT MOD_RES 1081
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1084
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 1089
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 1301
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1338
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1372
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BTM8"
FT MOD_RES 1459
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19367720,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1533
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1538
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BTM8"
FT MOD_RES 1630
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1734
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1835
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1967
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 2053
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 2128
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2152
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:25666618,
FT ECO:0000269|PubMed:26460884, ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 2158
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 2163
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 2180
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BTM8"
FT MOD_RES 2284
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 2327
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2329
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BTM8"
FT MOD_RES 2336
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:25666618,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 2338
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2370
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BTM8"
FT MOD_RES 2414
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 2510
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2523
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BTM8"
FT MOD_RES 2526
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BTM8"
FT MOD_RES 2569
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BTM8"
FT MOD_RES 2569
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BTM8"
FT MOD_RES 2575
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BTM8"
FT MOD_RES 2599
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8BTM8"
FT MOD_RES 2607
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 2621
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 42
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:24052262"
FT CROSSLNK 43
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:24052262"
FT CROSSLNK 135
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:24052262"
FT CROSSLNK 299
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 299
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1649..1656
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_035454"
FT VARIANT 39
FT /note="A -> G (in PVNH1; dbSNP:rs137853313)"
FT /evidence="ECO:0000269|PubMed:15668422"
FT /id="VAR_022734"
FT VARIANT 82
FT /note="E -> V (in PVNH1; dbSNP:rs28935169)"
FT /evidence="ECO:0000269|PubMed:11914408"
FT /id="VAR_015699"
FT VARIANT 102
FT /note="M -> V (in PVNH1)"
FT /evidence="ECO:0000269|PubMed:15249610"
FT /id="VAR_031305"
FT VARIANT 128
FT /note="A -> V (in PVNH1; dbSNP:rs137853315)"
FT /evidence="ECO:0000269|PubMed:15994863"
FT /id="VAR_031306"
FT VARIANT 149
FT /note="S -> F (in PVNH1)"
FT /evidence="ECO:0000269|PubMed:15249610"
FT /id="VAR_031307"
FT VARIANT 170
FT /note="Q -> P (in OPD2; dbSNP:rs863223628)"
FT /evidence="ECO:0000269|PubMed:12612583"
FT /id="VAR_015713"
FT VARIANT 172
FT /note="L -> F (in OPD1)"
FT /evidence="ECO:0000269|PubMed:12612583"
FT /id="VAR_015714"
FT VARIANT 187
FT /note="N -> S (in OPD2; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:27193221"
FT /id="VAR_076500"
FT VARIANT 196
FT /note="R -> G (in OPD2)"
FT /evidence="ECO:0000269|PubMed:12612583,
FT ECO:0000269|PubMed:27193221"
FT /id="VAR_015715"
FT VARIANT 196
FT /note="R -> W (in OPD1; dbSNP:rs137853317)"
FT /evidence="ECO:0000269|PubMed:12612583"
FT /id="VAR_015716"
FT VARIANT 200
FT /note="A -> S (in OPD2)"
FT /evidence="ECO:0000269|PubMed:12612583"
FT /id="VAR_015717"
FT VARIANT 203
FT /note="D -> Y (in OPD1; dbSNP:rs137853314)"
FT /evidence="ECO:0000269|PubMed:15940695"
FT /id="VAR_031308"
FT VARIANT 207
FT /note="P -> L (in OPD1; dbSNP:rs28935469)"
FT /evidence="ECO:0000269|PubMed:12612583,
FT ECO:0000269|PubMed:27193221"
FT /id="VAR_015700"
FT VARIANT 210
FT /note="C -> F (in OPD2; dbSNP:rs137853318)"
FT /evidence="ECO:0000269|PubMed:17431908"
FT /id="VAR_058720"
FT VARIANT 254
FT /note="E -> K (in OPD2; dbSNP:rs28935470)"
FT /evidence="ECO:0000269|PubMed:12612583"
FT /id="VAR_015701"
FT VARIANT 267
FT /note="A -> T (in OPD1; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:27193221"
FT /id="VAR_076501"
FT VARIANT 273
FT /note="A -> P (in OPD2)"
FT /evidence="ECO:0000269|PubMed:12612583"
FT /id="VAR_015718"
FT VARIANT 288
FT /note="G -> R (in CVD1; dbSNP:rs267606816)"
FT /evidence="ECO:0000269|PubMed:17190868"
FT /id="VAR_064156"
FT VARIANT 320
FT /note="V -> A (in dbSNP:rs1064816)"
FT /id="VAR_012831"
FT VARIANT 370
FT /note="F -> L (in dbSNP:rs1064817)"
FT /id="VAR_012832"
FT VARIANT 429
FT /note="T -> M (in dbSNP:rs36051194)"
FT /evidence="ECO:0000269|PubMed:12612583"
FT /id="VAR_069803"
FT VARIANT 528
FT /note="V -> M (in dbSNP:rs143873938)"
FT /evidence="ECO:0000269|PubMed:12410386,
FT ECO:0000269|PubMed:20844545"
FT /id="VAR_031309"
FT VARIANT 552
FT /note="V -> A (in dbSNP:rs730319)"
FT /id="VAR_012833"
FT VARIANT 555
FT /note="T -> K (in OPD2; dbSNP:rs782611953)"
FT /evidence="ECO:0000269|PubMed:12612583"
FT /id="VAR_015719"
FT VARIANT 606
FT /note="V -> L (found in a child with developmental
FT disabilities; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:30500825"
FT /id="VAR_085766"
FT VARIANT 637
FT /note="P -> Q (in CVD1; dbSNP:rs267606815)"
FT /evidence="ECO:0000269|PubMed:17190868"
FT /id="VAR_064157"
FT VARIANT 656
FT /note="L -> F (in PVNH1; dbSNP:rs137853311)"
FT /evidence="ECO:0000269|PubMed:11532987"
FT /id="VAR_012834"
FT VARIANT 711
FT /note="V -> D (in CVD1; dbSNP:rs267606817)"
FT /evidence="ECO:0000269|PubMed:17190868"
FT /id="VAR_064158"
FT VARIANT 804
FT /note="V -> D (in OPD1; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:27193221"
FT /id="VAR_076502"
FT VARIANT 1012
FT /note="S -> L (in dbSNP:rs17091204)"
FT /id="VAR_031310"
FT VARIANT 1142
FT /note="D -> V (in FMD1; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:27193221"
FT /id="VAR_076503"
FT VARIANT 1159
FT /note="D -> A (in FMD1; does not inhibit interaction with
FT MIS18BP1; dbSNP:rs28935471)"
FT /evidence="ECO:0000269|PubMed:12612583,
FT ECO:0000269|PubMed:21228480"
FT /id="VAR_015702"
FT VARIANT 1163
FT /note="V -> L (in MNS; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:27193221"
FT /id="VAR_076504"
FT VARIANT 1184
FT /note="D -> E (in MNS; dbSNP:rs80338837)"
FT /evidence="ECO:0000269|PubMed:12612583"
FT /id="VAR_015720"
FT VARIANT 1186
FT /note="S -> L (in FMD1; dbSNP:rs137853312)"
FT /evidence="ECO:0000269|PubMed:12612583,
FT ECO:0000269|PubMed:16596676, ECO:0000269|PubMed:27193221"
FT /id="VAR_015721"
FT VARIANT 1188
FT /note="A -> T (in MNS; does not inhibit interaction with
FT MIS18BP1; dbSNP:rs28935472)"
FT /evidence="ECO:0000269|PubMed:12612583,
FT ECO:0000269|PubMed:21228480, ECO:0000269|PubMed:27193221"
FT /id="VAR_015703"
FT VARIANT 1199
FT /note="S -> L (in MNS; does not inhibit interaction with
FT MIS18BP1; dbSNP:rs28935473)"
FT /evidence="ECO:0000269|PubMed:12612583,
FT ECO:0000269|PubMed:21228480"
FT /id="VAR_015704"
FT VARIANT 1291
FT /note="P -> L (in FGS2; dbSNP:rs137853319)"
FT /evidence="ECO:0000269|PubMed:17632775"
FT /id="VAR_058721"
FT VARIANT 1419
FT /note="A -> G (in dbSNP:rs35504556)"
FT /id="VAR_032083"
FT VARIANT 1620
FT /note="Missing (in FMD1)"
FT /evidence="ECO:0000269|PubMed:12612583"
FT /id="VAR_015722"
FT VARIANT 1635..1637
FT /note="Missing (in otopalatodigital spectrum disorder)"
FT /evidence="ECO:0000269|PubMed:15654694"
FT /id="VAR_031311"
FT VARIANT 1645
FT /note="C -> F (in OPD2)"
FT /evidence="ECO:0000269|PubMed:12612583"
FT /id="VAR_015723"
FT VARIANT 1724..1739
FT /note="Missing (in TOD)"
FT /evidence="ECO:0000269|PubMed:20598277"
FT /id="VAR_064159"
FT VARIANT 1728
FT /note="G -> C (in FMD1; dbSNP:rs137853316)"
FT /evidence="ECO:0000269|PubMed:16596676"
FT /id="VAR_031312"
FT VARIANT 1764
FT /note="A -> T (in dbSNP:rs57108893)"
FT /evidence="ECO:0000269|PubMed:11532987,
FT ECO:0000269|PubMed:12612583"
FT /id="VAR_012835"
FT VARIANT 1803
FT /note="E -> K (probable disease-associated variant found in
FT a patient with macrothrombocytopenia; dbSNP:rs368750879)"
FT /evidence="ECO:0000269|PubMed:21960593"
FT /id="VAR_067251"
FT VARIANT 1840
FT /note="H -> R (in FMD1; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:27193221"
FT /id="VAR_076505"
FT VARIANT 2391
FT /note="R -> H (in OPD1; unknown pathological significance;
FT dbSNP:rs727503930)"
FT /evidence="ECO:0000269|PubMed:27193221"
FT /id="VAR_076506"
FT MUTAGEN 42
FT /note="K->R: Abrogates ASB2alpha-mediated degradation
FT without altering ASB2alpha binding; when associated with R-
FT 43 and R-135."
FT /evidence="ECO:0000269|PubMed:24052262"
FT MUTAGEN 43
FT /note="K->R: Abrogates ASB2alpha-mediated degradation
FT without altering ASB2alpha binding; when associated with R-
FT 42 and R-135."
FT /evidence="ECO:0000269|PubMed:24052262"
FT MUTAGEN 135
FT /note="K->R: Abrogates ASB2alpha-mediated degradation
FT without altering ASB2alpha binding; when associated with R-
FT 42 and R-43."
FT /evidence="ECO:0000269|PubMed:24052262"
FT CONFLICT 44
FT /note="I -> T (in Ref. 10; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1772
FT /note="A -> G (in Ref. 11; CAA49687)"
FT /evidence="ECO:0000305"
FT CONFLICT 2341
FT /note="Q -> R (in Ref. 5; BAC03408)"
FT /evidence="ECO:0000305"
FT CONFLICT 2634
FT /note="D -> H (in Ref. 2; CAA37495)"
FT /evidence="ECO:0000305"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:3HOC"
FT HELIX 44..57
FT /evidence="ECO:0007829|PDB:3HOC"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:3HOC"
FT TURN 67..73
FT /evidence="ECO:0007829|PDB:3HOC"
FT HELIX 75..85
FT /evidence="ECO:0007829|PDB:3HOC"
FT HELIX 100..116
FT /evidence="ECO:0007829|PDB:3HOC"
FT HELIX 126..130
FT /evidence="ECO:0007829|PDB:3HOC"
FT HELIX 134..149
FT /evidence="ECO:0007829|PDB:3HOC"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:3HOP"
FT HELIX 168..179
FT /evidence="ECO:0007829|PDB:3HOC"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:3HOR"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:3HOC"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:3HOR"
FT HELIX 196..205
FT /evidence="ECO:0007829|PDB:3HOC"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:3HOC"
FT HELIX 221..236
FT /evidence="ECO:0007829|PDB:3HOC"
FT HELIX 244..247
FT /evidence="ECO:0007829|PDB:3HOC"
FT HELIX 254..261
FT /evidence="ECO:0007829|PDB:3HOC"
FT HELIX 263..266
FT /evidence="ECO:0007829|PDB:3HOP"
FT HELIX 480..482
FT /evidence="ECO:0007829|PDB:4M9P"
FT STRAND 484..487
FT /evidence="ECO:0007829|PDB:4M9P"
FT HELIX 488..490
FT /evidence="ECO:0007829|PDB:4M9P"
FT STRAND 501..506
FT /evidence="ECO:0007829|PDB:4M9P"
FT STRAND 515..521
FT /evidence="ECO:0007829|PDB:4M9P"
FT STRAND 529..534
FT /evidence="ECO:0007829|PDB:4M9P"
FT STRAND 537..542
FT /evidence="ECO:0007829|PDB:4M9P"
FT STRAND 548..556
FT /evidence="ECO:0007829|PDB:4M9P"
FT STRAND 565..571
FT /evidence="ECO:0007829|PDB:4M9P"
FT STRAND 579..583
FT /evidence="ECO:0007829|PDB:4M9P"
FT HELIX 584..586
FT /evidence="ECO:0007829|PDB:4M9P"
FT STRAND 588..590
FT /evidence="ECO:0007829|PDB:4M9P"
FT STRAND 595..604
FT /evidence="ECO:0007829|PDB:4M9P"
FT STRAND 609..617
FT /evidence="ECO:0007829|PDB:4M9P"
FT STRAND 620..625
FT /evidence="ECO:0007829|PDB:4M9P"
FT STRAND 627..636
FT /evidence="ECO:0007829|PDB:4M9P"
FT STRAND 639..649
FT /evidence="ECO:0007829|PDB:4M9P"
FT STRAND 658..664
FT /evidence="ECO:0007829|PDB:4M9P"
FT HELIX 672..674
FT /evidence="ECO:0007829|PDB:4M9P"
FT STRAND 676..679
FT /evidence="ECO:0007829|PDB:4M9P"
FT HELIX 680..682
FT /evidence="ECO:0007829|PDB:4M9P"
FT STRAND 683..685
FT /evidence="ECO:0007829|PDB:4M9P"
FT STRAND 693..698
FT /evidence="ECO:0007829|PDB:4M9P"
FT STRAND 707..712
FT /evidence="ECO:0007829|PDB:4M9P"
FT STRAND 714..716
FT /evidence="ECO:0007829|PDB:4M9P"
FT STRAND 721..725
FT /evidence="ECO:0007829|PDB:4M9P"
FT STRAND 727..735
FT /evidence="ECO:0007829|PDB:4M9P"
FT STRAND 739..749
FT /evidence="ECO:0007829|PDB:4M9P"
FT STRAND 758..762
FT /evidence="ECO:0007829|PDB:4M9P"
FT HELIX 1160..1162
FT /evidence="ECO:0007829|PDB:3RGH"
FT STRAND 1164..1167
FT /evidence="ECO:0007829|PDB:3RGH"
FT HELIX 1168..1170
FT /evidence="ECO:0007829|PDB:3RGH"
FT STRAND 1172..1174
FT /evidence="ECO:0007829|PDB:3RGH"
FT STRAND 1179..1184
FT /evidence="ECO:0007829|PDB:3RGH"
FT STRAND 1193..1198
FT /evidence="ECO:0007829|PDB:3RGH"
FT STRAND 1206..1211
FT /evidence="ECO:0007829|PDB:3RGH"
FT STRAND 1213..1222
FT /evidence="ECO:0007829|PDB:3RGH"
FT STRAND 1225..1235
FT /evidence="ECO:0007829|PDB:3RGH"
FT STRAND 1244..1250
FT /evidence="ECO:0007829|PDB:3RGH"
FT TURN 1785..1787
FT /evidence="ECO:0007829|PDB:2K7P"
FT STRAND 1791..1796
FT /evidence="ECO:0007829|PDB:2K7P"
FT STRAND 1804..1809
FT /evidence="ECO:0007829|PDB:2K7P"
FT STRAND 1819..1822
FT /evidence="ECO:0007829|PDB:2K7P"
FT STRAND 1824..1832
FT /evidence="ECO:0007829|PDB:2K7P"
FT STRAND 1838..1846
FT /evidence="ECO:0007829|PDB:2K7P"
FT STRAND 1855..1860
FT /evidence="ECO:0007829|PDB:2K7P"
FT STRAND 1865..1867
FT /evidence="ECO:0007829|PDB:2K7P"
FT STRAND 1869..1872
FT /evidence="ECO:0007829|PDB:2BP3"
FT HELIX 1873..1875
FT /evidence="ECO:0007829|PDB:2BP3"
FT STRAND 1877..1879
FT /evidence="ECO:0007829|PDB:2BP3"
FT STRAND 1884..1889
FT /evidence="ECO:0007829|PDB:2BP3"
FT TURN 1891..1893
FT /evidence="ECO:0007829|PDB:2AAV"
FT STRAND 1895..1906
FT /evidence="ECO:0007829|PDB:2BP3"
FT STRAND 1909..1914
FT /evidence="ECO:0007829|PDB:2BP3"
FT STRAND 1916..1925
FT /evidence="ECO:0007829|PDB:2BP3"
FT STRAND 1930..1938
FT /evidence="ECO:0007829|PDB:2BP3"
FT STRAND 1947..1953
FT /evidence="ECO:0007829|PDB:2BP3"
FT STRAND 1959..1967
FT /evidence="ECO:0007829|PDB:2K7Q"
FT STRAND 1980..1988
FT /evidence="ECO:0007829|PDB:2K7Q"
FT STRAND 1998..2001
FT /evidence="ECO:0007829|PDB:2K7Q"
FT STRAND 2007..2010
FT /evidence="ECO:0007829|PDB:2K7Q"
FT STRAND 2014..2025
FT /evidence="ECO:0007829|PDB:2K7Q"
FT STRAND 2034..2039
FT /evidence="ECO:0007829|PDB:2K7Q"
FT HELIX 2041..2043
FT /evidence="ECO:0007829|PDB:2K7Q"
FT HELIX 2047..2049
FT /evidence="ECO:0007829|PDB:2J3S"
FT STRAND 2051..2054
FT /evidence="ECO:0007829|PDB:2J3S"
FT HELIX 2055..2057
FT /evidence="ECO:0007829|PDB:2J3S"
FT STRAND 2059..2061
FT /evidence="ECO:0007829|PDB:2J3S"
FT STRAND 2066..2071
FT /evidence="ECO:0007829|PDB:2J3S"
FT STRAND 2075..2077
FT /evidence="ECO:0007829|PDB:2J3S"
FT STRAND 2080..2088
FT /evidence="ECO:0007829|PDB:2J3S"
FT STRAND 2091..2096
FT /evidence="ECO:0007829|PDB:2J3S"
FT STRAND 2100..2107
FT /evidence="ECO:0007829|PDB:2J3S"
FT STRAND 2112..2120
FT /evidence="ECO:0007829|PDB:2J3S"
FT STRAND 2129..2136
FT /evidence="ECO:0007829|PDB:2J3S"
FT STRAND 2139..2148
FT /evidence="ECO:0007829|PDB:2J3S"
FT STRAND 2161..2165
FT /evidence="ECO:0007829|PDB:4P3W"
FT HELIX 2171..2173
FT /evidence="ECO:0007829|PDB:4P3W"
FT STRAND 2174..2179
FT /evidence="ECO:0007829|PDB:4P3W"
FT STRAND 2185..2187
FT /evidence="ECO:0007829|PDB:4P3W"
FT STRAND 2189..2192
FT /evidence="ECO:0007829|PDB:4P3W"
FT STRAND 2194..2201
FT /evidence="ECO:0007829|PDB:4P3W"
FT STRAND 2208..2216
FT /evidence="ECO:0007829|PDB:4P3W"
FT STRAND 2225..2229
FT /evidence="ECO:0007829|PDB:4P3W"
FT STRAND 2234..2236
FT /evidence="ECO:0007829|PDB:4P3W"
FT HELIX 2238..2240
FT /evidence="ECO:0007829|PDB:2W0P"
FT STRAND 2242..2245
FT /evidence="ECO:0007829|PDB:2W0P"
FT HELIX 2246..2248
FT /evidence="ECO:0007829|PDB:2W0P"
FT STRAND 2251..2253
FT /evidence="ECO:0007829|PDB:5XR1"
FT STRAND 2257..2262
FT /evidence="ECO:0007829|PDB:2W0P"
FT HELIX 2264..2266
FT /evidence="ECO:0007829|PDB:2W0P"
FT STRAND 2271..2279
FT /evidence="ECO:0007829|PDB:2W0P"
FT STRAND 2282..2287
FT /evidence="ECO:0007829|PDB:2W0P"
FT STRAND 2293..2298
FT /evidence="ECO:0007829|PDB:2W0P"
FT STRAND 2303..2311
FT /evidence="ECO:0007829|PDB:2W0P"
FT TURN 2316..2318
FT /evidence="ECO:0007829|PDB:5XR1"
FT STRAND 2320..2326
FT /evidence="ECO:0007829|PDB:2W0P"
FT TURN 2429..2431
FT /evidence="ECO:0007829|PDB:2K3T"
FT STRAND 2433..2436
FT /evidence="ECO:0007829|PDB:2K3T"
FT HELIX 2437..2439
FT /evidence="ECO:0007829|PDB:2K3T"
FT STRAND 2441..2443
FT /evidence="ECO:0007829|PDB:2K3T"
FT STRAND 2448..2453
FT /evidence="ECO:0007829|PDB:2K3T"
FT TURN 2455..2457
FT /evidence="ECO:0007829|PDB:2K3T"
FT STRAND 2462..2470
FT /evidence="ECO:0007829|PDB:2K3T"
FT STRAND 2472..2479
FT /evidence="ECO:0007829|PDB:2K3T"
FT STRAND 2482..2489
FT /evidence="ECO:0007829|PDB:2K3T"
FT STRAND 2491..2506
FT /evidence="ECO:0007829|PDB:2K3T"
FT STRAND 2511..2518
FT /evidence="ECO:0007829|PDB:2K3T"
FT STRAND 2561..2564
FT /evidence="ECO:0007829|PDB:3CNK"
FT HELIX 2565..2567
FT /evidence="ECO:0007829|PDB:3CNK"
FT STRAND 2576..2581
FT /evidence="ECO:0007829|PDB:3CNK"
FT STRAND 2590..2595
FT /evidence="ECO:0007829|PDB:3CNK"
FT STRAND 2597..2599
FT /evidence="ECO:0007829|PDB:3CNK"
FT STRAND 2602..2610
FT /evidence="ECO:0007829|PDB:3CNK"
FT STRAND 2613..2619
FT /evidence="ECO:0007829|PDB:3CNK"
FT STRAND 2624..2632
FT /evidence="ECO:0007829|PDB:3CNK"
FT STRAND 2641..2646
FT /evidence="ECO:0007829|PDB:3CNK"
SQ SEQUENCE 2647 AA; 280739 MW; 6C1A07041DF50142 CRC64;
MSSSHSRAGQ SAAGAAPGGG VDTRDAEMPA TEKDLAEDAP WKKIQQNTFT RWCNEHLKCV
SKRIANLQTD LSDGLRLIAL LEVLSQKKMH RKHNQRPTFR QMQLENVSVA LEFLDRESIK
LVSIDSKAIV DGNLKLILGL IWTLILHYSI SMPMWDEEED EEAKKQTPKQ RLLGWIQNKL
PQLPITNFSR DWQSGRALGA LVDSCAPGLC PDWDSWDASK PVTNAREAMQ QADDWLGIPQ
VITPEEIVDP NVDEHSVMTY LSQFPKAKLK PGAPLRPKLN PKKARAYGPG IEPTGNMVKK
RAEFTVETRS AGQGEVLVYV EDPAGHQEEA KVTANNDKNR TFSVWYVPEV TGTHKVTVLF
AGQHIAKSPF EVYVDKSQGD ASKVTAQGPG LEPSGNIANK TTYFEIFTAG AGTGEVEVVI
QDPMGQKGTV EPQLEARGDS TYRCSYQPTM EGVHTVHVTF AGVPIPRSPY TVTVGQACNP
SACRAVGRGL QPKGVRVKET ADFKVYTKGA GSGELKVTVK GPKGEERVKQ KDLGDGVYGF
EYYPMVPGTY IVTITWGGQN IGRSPFEVKV GTECGNQKVR AWGPGLEGGV VGKSADFVVE
AIGDDVGTLG FSVEGPSQAK IECDDKGDGS CDVRYWPQEA GEYAVHVLCN SEDIRLSPFM
ADIRDAPQDF HPDRVKARGP GLEKTGVAVN KPAEFTVDAK HGGKAPLRVQ VQDNEGCPVE
ALVKDNGNGT YSCSYVPRKP VKHTAMVSWG GVSIPNSPFR VNVGAGSHPN KVKVYGPGVA
KTGLKAHEPT YFTVDCAEAG QGDVSIGIKC APGVVGPAEA DIDFDIIRND NDTFTVKYTP
RGAGSYTIMV LFADQATPTS PIRVKVEPSH DASKVKAEGP GLSRTGVELG KPTHFTVNAK
AAGKGKLDVQ FSGLTKGDAV RDVDIIDHHD NTYTVKYTPV QQGPVGVNVT YGGDPIPKSP
FSVAVSPSLD LSKIKVSGLG EKVDVGKDQE FTVKSKGAGG QGKVASKIVG PSGAAVPCKV
EPGLGADNSV VRFLPREEGP YEVEVTYDGV PVPGSPFPLE AVAPTKPSKV KAFGPGLQGG
SAGSPARFTI DTKGAGTGGL GLTVEGPCEA QLECLDNGDG TCSVSYVPTE PGDYNINILF
ADTHIPGSPF KAHVVPCFDA SKVKCSGPGL ERATAGEVGQ FQVDCSSAGS AELTIEICSE
AGLPAEVYIQ DHGDGTHTIT YIPLCPGAYT VTIKYGGQPV PNFPSKLQVE PAVDTSGVQC
YGPGIEGQGV FREATTEFSV DARALTQTGG PHVKARVANP SGNLTETYVQ DRGDGMYKVE
YTPYEEGLHS VDVTYDGSPV PSSPFQVPVT EGCDPSRVRV HGPGIQSGTT NKPNKFTVET
RGAGTGGLGL AVEGPSEAKM SCMDNKDGSC SVEYIPYEAG TYSLNVTYGG HQVPGSPFKV
PVHDVTDASK VKCSGPGLSP GMVRANLPQS FQVDTSKAGV APLQVKVQGP KGLVEPVDVV
DNADGTQTVN YVPSREGPYS ISVLYGDEEV PRSPFKVKVL PTHDASKVKA SGPGLNTTGV
PASLPVEFTI DAKDAGEGLL AVQITDPEGK PKKTHIQDNH DGTYTVAYVP DVTGRYTILI
KYGGDEIPFS PYRVRAVPTG DASKCTVTVS IGGHGLGAGI GPTIQIGEET VITVDTKAAG
KGKVTCTVCT PDGSEVDVDV VENEDGTFDI FYTAPQPGKY VICVRFGGEH VPNSPFQVTA
LAGDQPSVQP PLRSQQLAPQ YTYAQGGQQT WAPERPLVGV NGLDVTSLRP FDLVIPFTIK
KGEITGEVRM PSGKVAQPTI TDNKDGTVTV RYAPSEAGLH EMDIRYDNMH IPGSPLQFYV
DYVNCGHVTA YGPGLTHGVV NKPATFTVNT KDAGEGGLSL AIEGPSKAEI SCTDNQDGTC
SVSYLPVLPG DYSILVKYNE QHVPGSPFTA RVTGDDSMRM SHLKVGSAAD IPINISETDL
SLLTATVVPP SGREEPCLLK RLRNGHVGIS FVPKETGEHL VHVKKNGQHV ASSPIPVVIS
QSEIGDASRV RVSGQGLHEG HTFEPAEFII DTRDAGYGGL SLSIEGPSKV DINTEDLEDG
TCRVTYCPTE PGNYIINIKF ADQHVPGSPF SVKVTGEGRV KESITRRRRA PSVANVGSHC
DLSLKIPEIS IQDMTAQVTS PSGKTHEAEI VEGENHTYCI RFVPAEMGTH TVSVKYKGQH
VPGSPFQFTV GPLGEGGAHK VRAGGPGLER AEAGVPAEFS IWTREAGAGG LAIAVEGPSK
AEISFEDRKD GSCGVAYVVQ EPGDYEVSVK FNEEHIPDSP FVVPVASPSG DARRLTVSSL
QESGLKVNQP ASFAVSLNGA KGAIDAKVHS PSGALEECYV TEIDQDKYAV RFIPRENGVY
LIDVKFNGTH IPGSPFKIRV GEPGHGGDPG LVSAYGAGLE GGVTGNPAEF VVNTSNAGAG
ALSVTIDGPS KVKMDCQECP EGYRVTYTPM APGSYLISIK YGGPYHIGGS PFKAKVTGPR
LVSNHSLHET SSVFVDSLTK ATCAPQHGAP GPGPADASKV VAKGLGLSKA YVGQKSSFTV
DCSKAGNNML LVGVHGPRTP CEEILVKHVG SRLYSVSYLL KDKGEYTLVV KWGDEHIPGS
PYRVVVP
